Biopolymers projects

Biopolymers exhibit structure and function at the individual protein level and at the scale of assemblies such as filaments and assemblies of filaments. We are interested in how (i) intrinsic disorder (ii) chirality and (iii) surface interactions are responsible for function in protein biopolymers.

At the molecular level, we have studied, for example, using explicit atomically detailed computer simulations protein filaments such as FtsZ which aid in bacterial cell division and we have shown that flexibility in the protein can produce mechanical forces. Geometric incompatibility between such filaments and the surfaces to which they bind can also result in novel physics including geometry controlled switching of protein filament conformations .

Intrinsically disordered proteins can extract function from entropy. Entropically driven processes such as translocation are important for disordered proteins and are sensitive to the surrounding geometry and crowding. Intrinsic disorder also plays a role in events at the cellular level such as the transport of cargo from the nucleus to cytoplasm and vice versa through the nuclear pore complex - one of the biggest macromolecular gates in your bodies made of hundreds of proteins. We have shown, using appropriately coarse-grained simulations and analytical theory that interactions between the cargo and a higher order organization of the proteins in the pore can lead to the opening and closing of the pore, pointing to a novel way of gating channels.

Representative papers on some of these topics are below:

"Cooperative interactions between different classes of disordered proteins play a functional role in the nuclear pore complex of Baker’s yeast", D. Ando, A. Gopinathan, PLoS ONE 12(1): e0169455 (2017)